| No. Registro | 001265304 |
| Tipo de material | ARTIGO DE PERIODICO - INTERNACIONAL |
| Cód. publicação |  10.1016/s0006-2952(02)01210-8 DOI |
| Entrada Principal | Andrião-Escarso, Sílvia Helena (**) |
| Título | Structural and functional characterization of an acidic platelet aggregation inhibitor and hypotensive phospholipase ’A IND.2’ from Bothrops jararacussu snake venom. |
| Imprenta | New York, 2002. |
| Descrição | p. 723-732. |
| Idioma | Inglês |
| Assunto | BIOQUÍMICA |
| | FARMACOLOGIA |
| | VENENOS DE ORIGEM ANIMAL |
| Autor Secundário | Soares, Andreimar Martins (*) |
| | Fontes, Marcos Roberto de Mattos (*) NAC Depto. de Física e Biofísica, IB, Universidade Estadual Paulista, Botucatu-SP |
| | Fuly, André L. (*) NAC Departamento de Bioquímica Médica, Centro de Ciências da Saúde, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ |
| | Corrêa, Fernando Morgan de Aguiar |
| | Rosa, José C. (*) |
| | Greene, Lewis Joel |
| | Giglio, José Roberto (*) |
| Fonte | In: Biochemical Pharmacology, New York, v. 64, p. 723-732, 2002, ISSN: 0006-2952 |
| Localiz.Eletrônica | e-mail do autor -- mailto://jrgiglio@fmrp.usp.br |
| Localiz.Eletrônica |
 Acesso para publicação em formato eletrônico |
| Resumo/Outros | An acidic (pI’DA ORDEM DE’4.5) phospholipase ’A IND. 2’ (BthA-I-PL’A IND.2’) was isolated from Bothrops jararacussu snake venom by ion-exchange chromatography on a CM-Sepharose column followed by reverse phase chromatography on an RP-HPLC C-18 column. It is an ’DA ORDEM DE’13.7 kDa single chain Asp49 PL’A IND.2’ with approximately 122 amino acid residues, 7 disulfide bridges, and the following N-terminal sequence: ’ANTPOT.1 SLWQFGKMINYVM-GESGVLQYLSYGCYCGLGGQGQPTDATDRCCFVHDCC’ POT.51’. Crystals of this acidic protein diffracted beyond 2.0 ’ângstron’ resolution. These crystals are monoclinic and have unit cell dimensions of a=33.9, b=63.8, c=49.1 ’ângstron’, and ’beta’=104.0’GRAUS’. Although not myotoxic, cytotoxic, or lethal, the protein was catalytically 3-4 times more active than BthTX-II, a basic D49 myotoxic PL’A IND.2’ from the same venom and other Bothrops venoms. Although it showed no toxic activity, it was able to induce time-independent edema, this activity being inhibited by EDTA. In addition, BthA-I-PL’A IND.2’ caused a hypotensive response in the rat and inhibited platelet aggregation. Catalytic, antiplatelet and other activities were abolished by chemical modification with 4-bromophenacyl bromide, which is known to covalently bind to His48 of the catalytic site. Antibodies raised against crude B. jararacussu venom recognized this acidic PL’A IND.2’, while anti-Asp49-BthTX-II recognized it weakly and anti-Lys49-BthTX-I showed the least |
| | cross-reaction. These data confirm that myotoxicity does not necessarily correlate with catalytic activity in native PL’A IND.2’ homologues and that either of these two activities may exist alone. BthA-I-PLA2, in addition to representing a relevant molecular model of catalytic activity, is also a promising hypotensive agent and platelet aggregation inhibitor for further studies |
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| Acervo Geral | Todos os itens |
| Itens na Biblioteca | BCRP-Fac Medicina Rib Preto |
| Unidade USP | FMRP -- FAC DE MEDICINA DE RIBEIRÃO PRETO |
| | FMRP -- FAC DE MEDICINA DE RIBEIRÃO PRETO |
| | FMRP -- FAC DE MEDICINA DE RIBEIRÃO PRETO |
| | FMRP -- FAC DE MEDICINA DE RIBEIRÃO PRETO |
| | FMRP -- FAC DE MEDICINA DE RIBEIRÃO PRETO |
